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6n84

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Current revision

MBP-fusion protein of transducin-alpha residues 327-350

Structural highlights

6n84 is a 1 chain structure with sequence from Escherichia coli O157:H7 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.75Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

GNAT2_HUMAN Progressive cone dystrophy;Achromatopsia. The disease is caused by variants affecting the gene represented in this entry.

Function

MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.GNAT2_HUMAN Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase.

Publication Abstract from PubMed

Resistance to inhibitors of cholinesterase 8A (Ric8A) is an essential regulator of G protein alpha-subunits (Galpha), acting as a guanine nucleotide exchange factor and a chaperone. We report two crystal structures of Ric8A, one in the apo form and the other in complex with a tagged C-terminal fragment of Galpha. These structures reveal two principal domains of Ric8A: an armadillo-fold core and a flexible C-terminal tail. Additionally, they show that the Galpha C-terminus binds to a highly-conserved patch on the concave surface of the Ric8A armadillo-domain, with selectivity determinants residing in the Galpha sequence. Biochemical analysis shows that the Ric8A C-terminal tail is critical for its stability and function. A model of the Ric8A/Galpha complex derived from crosslinking mass spectrometry and molecular dynamics simulations suggests that the Ric8A C-terminal tail helps organize the GTP-binding site of Galpha. This study lays the groundwork for understanding Ric8A function at the molecular level.

Structural underpinnings of Ric8A function as a G-protein alpha-subunit chaperone and guanine-nucleotide exchange factor.,Srivastava D, Gakhar L, Artemyev NO Nat Commun. 2019 Jul 12;10(1):3084. doi: 10.1038/s41467-019-11088-x. PMID:31300652^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Srivastava D, Gakhar L, Artemyev NO. Structural underpinnings of Ric8A function as a G-protein alpha-subunit chaperone and guanine-nucleotide exchange factor. Nat Commun. 2019 Jul 12;10(1):3084. doi: 10.1038/s41467-019-11088-x. PMID:31300652 doi:http://dx.doi.org/10.1038/s41467-019-11088-x

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6n84"

@@ Line 3: / Line 3: @@
 <StructureSection load='6n84' size='340' side='right'caption='[[6n84]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6n84]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N84 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N84 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6n84]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N84 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N84 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GNAT2, GNATC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6n84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n84 OCA], [http://pdbe.org/6n84 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n84 RCSB], [http://www.ebi.ac.uk/pdbsum/6n84 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n84 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6n84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n84 OCA], [https://pdbe.org/6n84 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n84 RCSB], [https://www.ebi.ac.uk/pdbsum/6n84 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n84 ProSAT]</span></td></tr>
 </table>
+== Disease ==
+[https://www.uniprot.org/uniprot/GNAT2_HUMAN GNAT2_HUMAN] Progressive cone dystrophy;Achromatopsia. The disease is caused by variants affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/MALE_ECO57 MALE_ECO57]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides (By similarity).
+[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/GNAT2_HUMAN GNAT2_HUMAN] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Escherichia coli O157:H7]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Artemyev, N O]]
+[[Category: Artemyev NO]]
-[[Category: Gakhar, L]]
+[[Category: Gakhar L]]
-[[Category: Srivastava, D]]
+[[Category: Srivastava D]]
-[[Category: Chaperone]]
-[[Category: G alpha]]
-[[Category: Mbp]]

6n84

From Proteopedia

Current revision

MBP-fusion protein of transducin-alpha residues 327-350

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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